5ogk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='5ogk' size='340' side='right' caption='[[5ogk]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='5ogk' size='340' side='right' caption='[[5ogk]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5ogk]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OGK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5ogk]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OGK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDD:GUANOSINE-5-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDD:GUANOSINE-5-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VRG4, GOG5, LDB3, MCD3, VAN2, VIG4, YGL225W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ogk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ogk OCA], [http://pdbe.org/5ogk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ogk RCSB], [http://www.ebi.ac.uk/pdbsum/5ogk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ogk ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ogk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ogk OCA], [http://pdbe.org/5ogk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ogk RCSB], [http://www.ebi.ac.uk/pdbsum/5ogk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ogk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GMT1_YEAST GMT1_YEAST]] Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Defective copy causes severe glycosylation defect and abnormal retention of soluble endoplasmic reticulum proteins. Involved in vanadate sensitivity.<ref>PMID:10570930</ref> <ref>PMID:11067855</ref> <ref>PMID:12478588</ref> <ref>PMID:15494368</ref> <ref>PMID:2014241</ref> <ref>PMID:2137555</ref> <ref>PMID:7672592</ref> <ref>PMID:7877969</ref> <ref>PMID:8632002</ref> <ref>PMID:9184829</ref> <ref>PMID:9335583</ref> <ref>PMID:9395539</ref>
[[http://www.uniprot.org/uniprot/GMT1_YEAST GMT1_YEAST]] Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Defective copy causes severe glycosylation defect and abnormal retention of soluble endoplasmic reticulum proteins. Involved in vanadate sensitivity.<ref>PMID:10570930</ref> <ref>PMID:11067855</ref> <ref>PMID:12478588</ref> <ref>PMID:15494368</ref> <ref>PMID:2014241</ref> <ref>PMID:2137555</ref> <ref>PMID:7672592</ref> <ref>PMID:7877969</ref> <ref>PMID:8632002</ref> <ref>PMID:9184829</ref> <ref>PMID:9335583</ref> <ref>PMID:9395539</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Glycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for the glycosyltransferases. NSTs are linked to several developmental and immune disorders in humans, and in pathogenic microbes they have an important role in virulence. How NSTs recognize and transport activated monosaccharides, however, is currently unclear. Here we present the crystal structure of an NST, the GDP-mannose transporter Vrg4, in both the substrate-free and the bound states. A hitherto unobserved requirement of short-chain lipids in activating the transporter supports a model for regulation within the highly dynamic membranes of the Golgi apparatus. Our results provide a structural basis for understanding nucleotide sugar recognition, and provide insights into the transport and regulatory mechanism of this family of intracellular transporters.
 +
 +
Structural basis of nucleotide sugar transport across the Golgi membrane.,Parker JL, Newstead S Nature. 2017 Nov 23;551(7681):521-524. doi: 10.1038/nature24464. Epub 2017 Nov, 15. PMID:29143814<ref>PMID:29143814</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5ogk" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Baker's yeast]]
[[Category: Newstead, S]]
[[Category: Newstead, S]]
[[Category: Parker, J L]]
[[Category: Parker, J L]]

Revision as of 07:30, 29 November 2017

Crystal structure of a nucleotide sugar transporter with bound nucleotide sugar.

5ogk, resolution 3.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools